Abstract
The primary structure of lipopolysaccharide binding protein (LBP), a trace plasma protein that binds to the lipid A moiety of bacterial lipopolysaccharides (LPSs), was deduced by sequencing cloned complementary DNA. LBP shares sequence identity with another LPS binding protein found in granulocytes, bactericidal/permeability-increasing protein, and with cholesterol ester transport protein of the plasma. LBP may control the response to LPS under physiologic conditions by forming high-affinity complexes with LPS that bind to monocytes and macrophages, which then secrete tumor necrosis factor. The identification of this pathway for LPS-induced monocyte stimulation may aid in the development of treatments for diseases in which Gram-negative sepsis or endotoxemia are involved.
Publication types
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Comparative Study
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Acute-Phase Proteins*
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Amino Acid Sequence
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Animals
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Base Sequence
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Blood Proteins / genetics*
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Carrier Proteins / genetics*
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Carrier Proteins / metabolism
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Gene Library
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Humans
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Kinetics
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Lipid A / metabolism
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Lipopolysaccharides / metabolism*
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Lipopolysaccharides / pharmacology
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Male
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Membrane Glycoproteins*
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Molecular Sequence Data
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Oligonucleotide Probes
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Rabbits
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Sequence Homology, Nucleic Acid
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Sheep
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Staphylococcus aureus
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Tumor Necrosis Factor-alpha / biosynthesis
Substances
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Acute-Phase Proteins
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Blood Proteins
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Carrier Proteins
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Lipid A
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Lipopolysaccharides
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Membrane Glycoproteins
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Oligonucleotide Probes
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Tumor Necrosis Factor-alpha
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lipopolysaccharide-binding protein
Associated data
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GENBANK/M35533
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GENBANK/M35534